3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy

Xuekui Yu, Lei Jin and Z. Hong Zhou ()
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Xuekui Yu: The University of Texas Medical School at Houston, Houston, Texas 77030, USA
Lei Jin: The University of Texas Medical School at Houston, Houston, Texas 77030, USA
Z. Hong Zhou: The University of Texas Medical School at Houston, Houston, Texas 77030, USA

Nature, 2008, vol. 453, issue 7193, 415-419

Abstract: Cytoplasmic polyhedrosis virus Cytoplasmic polyhedrosis virus (CPV) is a member of a large family of double-stranded RNA viruses, but it is unique in having a single shell capsid yet being fully capable of cell entry and mRNA transcription. The structure of this virus has now been determined by single-particle cryo-electron microscopy (cryoEM) to a resolution of 3.88 Å. The technique allows the polypeptide backbone to be traced without the need to make a crystal. The high-resolution structure shows how conformational switching is exploited to make railroad-like 'sliding' tracks for RNA packing and transcription and reveals an mRNA releasing hole coupled with distinctive capping machinery. With this and several other recent publications, cryo-electron microscopy underlines its credentials as a system capable of atomic-resolution in structural studies.

Date: 2008
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DOI: 10.1038/nature06893

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